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HIS7_XANCB
ID   HIS7_XANCB              Reviewed;         375 AA.
AC   B0RSL6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Histidine biosynthesis bifunctional protein HisB {ECO:0000255|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Histidinol-phosphatase {ECO:0000255|HAMAP-Rule:MF_01022};
DE              EC=3.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_01022};
DE              Short=IGPD {ECO:0000255|HAMAP-Rule:MF_01022};
DE              EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_01022};
GN   Name=hisB {ECO:0000255|HAMAP-Rule:MF_01022};
GN   OrderedLocusNames=xcc-b100_2098;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-
CC         4-yl)-2-oxopropyl phosphate + H2O; Xref=Rhea:RHEA:11040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57766, ChEBI:CHEBI:58278; EC=4.2.1.19;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01022};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidinol phosphate = L-histidinol + phosphate;
CC         Xref=Rhea:RHEA:14465, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57699, ChEBI:CHEBI:57980; EC=3.1.3.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01022};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01022};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the histidinol-
CC       phosphatase family. {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       imidazoleglycerol-phosphate dehydratase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01022}.
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DR   EMBL; AM920689; CAP51451.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RSL6; -.
DR   SMR; B0RSL6; -.
DR   KEGG; xca:xcc-b100_2098; -.
DR   HOGENOM; CLU_044308_0_0_6; -.
DR   OMA; PEDTFWP; -.
DR   UniPathway; UPA00031; UER00011.
DR   UniPathway; UPA00031; UER00013.
DR   Proteomes; UP000001188; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07914; IGPD; 1.
DR   Gene3D; 3.30.230.40; -; 2.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_01022; Bifunc_HisB; 1.
DR   HAMAP; MF_00076; HisB; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR020566; His_synth_bifunc_HisB.
DR   InterPro; IPR005954; HisB_N.
DR   InterPro; IPR006543; Histidinol-phos.
DR   InterPro; IPR038494; IGPD_sf.
DR   InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR   InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR23133; PTHR23133; 1.
DR   Pfam; PF00475; IGPD; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01261; hisB_Nterm; 1.
DR   TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
DR   PROSITE; PS00954; IGP_DEHYDRATASE_1; 1.
DR   PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Hydrolase;
KW   Lyase; Magnesium; Metal-binding; Multifunctional enzyme.
FT   CHAIN           1..375
FT                   /note="Histidine biosynthesis bifunctional protein HisB"
FT                   /id="PRO_1000135372"
FT   REGION          1..168
FT                   /note="Histidinol-phosphatase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   REGION          169..375
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   ACT_SITE        10
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
SQ   SEQUENCE   375 AA;  41780 MW;  AC9A9B064F19B5EB CRC64;
     MTPILFVDRD GTLITEPADF QIDAYEKLRF VEGVIPAMLK LRDAGYQFVI VSNQDGLGSE
     SYPQASFDGP NNLMLQIFAS QGIVFREVLI DCSWPADNAP TRKPGVGLMV PYLQDRTIDW
     SRSAMVGDRI TDIQFAQNLN IRGFQLRTEQ FGGDWDWAGI AHELADAPRR AVVQRNTKET
     RIRVELDLDR VAEPHTATGL PFFDHMLEQI GKHGGFALDI RAEGDLHIDE HHTIEDTGLA
     LGQALREALG DKRGIGRYGF DPVDSPWRVA GDTAQHGFTL PMDETIASAA LDFSGRPYFV
     FDGDFKRERV GDMPTELVPH FFRSVCDASG LNLHLHVRGE NDHHKVEGCF KALARALRQA
     IRREGTALPS TKGAL
 
 
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